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P80543 - MDH_BREVE
- Names & Taxonomy
- Subcellular locationSubcell. location
- Pathology & BiotechPathol./Biotech
- PTM / Processing
- Family & Domains
- Entry information
- BLAST>sp|P80543|MDH_BREVE Malate dehydrogenase (Fragment) OS=Brevundimonas vesicularis GN=mdh PE=1 SV=1 AXAKIALIGAGMIGGTLAA
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Select a section on the left to see content.Catalyzes the reversible oxidation of malate to oxaloacetate.By similarity(S)-malate + NAD+ = oxaloacetate + NADH.
Feature key Position(s) Length Description Graphical view Feature identifier Actions <p>Describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.</p><p><a href='../manual/np_bind' target='_top'>More...</a></p>Nucleotide bindingi 9 – 14 6 NADBy similarity
- L-malate dehydrogenase activity Source: UniProtKB-EC
- tricarboxylic acid cycle Source: UniProtKB-KW
<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Biological processiTricarboxylic acid cycleRecommended name:Malate dehydrogenase (EC:184.108.40.206)Name:mdh
Brevundimonas vesicularis (Pseudomonas vesicularis) 41276 [NCBI] cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Caulobacterales › Caulobacteraceae › Brevundimonas
Feature key Position(s) Length Description Graphical view Feature identifier Actions 1 – ›19 ›19 Malate dehydrogenase PRO_0000113441 Add
<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusi: Fragment.Length:19Mass (Da):1,710Last modified:February 1, 1996 - v1<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3E643277AB542F23
Feature key Position(s) Length Description Graphical view Feature identifier Actions <p>Is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.</p><p><a href='../manual/non_ter' target='_top'>More...</a></p>Non-terminal residuei 19 – 19 1
3D structure databases
Database of comparative protein structure models<br/><a href='/database/63'>More..</a> ModBasei Search... Search...
Protocols and materials databases
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Family and domain databases
- "Structural studies of malate dehydrogenases (MDHs): MDHs in Brevundimonas species are the first reported MDHs in Proteobacteria which resemble lactate dehydrogenases in primary structure."
J. Bacteriol. 179:4066-4070(1997) [PubMed] [Europe PMC] [Abstract]Cited for: PROTEIN SEQUENCE.Strain: ATCC 11426 / DSM 7226 / JCM 1477 / LMG 2350 / NBRC 12165 / NCIMB 1945 / NCTC 10900.
MDH_BREVE P80543Primary (citable) accession number: P80543 Integrated into UniProtKB/Swiss-Prot: February 1, 1996 Last sequence update: February 1, 1996 Last modified: October 1, 2014 This is version 46 of the entry and version 1 of the sequence. [Complete history] Reviewed (UniProtKB/Swiss-Prot) Annotation program Prokaryotic Protein Annotation Program
- SIMILARITY commentsIndex of protein domains and families
External DataDasty 3